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The chloroplast ATP synthetase consist of the subunits α, β, γ, δ, ϵ and proteolipid only
Author(s) -
Süss Karl-Heinz,
Manteuffel Renate
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80134-3
Subject(s) - thylakoid , protein subunit , chloroplast , immunoprecipitation , biochemistry , biology , microbiology and biotechnology , gene
The subunit stoichiometry of the ATP synthetase (CF 1 ‐CF 0 ) immunoprecipitated from Triton X‐100 extracts of chloroplast thylakoid membranes was determined to be α 3 , β 3 , γ, δ, ϵ (CF 1 ) and I 0.3 , II 0.6–0.9 , III 4(6) (CF 0 ). Antibodies against the polypeptides α, β, γ, δ, I, II and ϵ combined specifically with the isolated subunits as analysed by the protein blotting method. Applying this technique, antibodies against the CF 1 subunits were found to form complexes with the corresponding polypeptides of thylakoids, whereas those against I ( M r 20 000) and II ( M r 17 000) combined with M r 26 000 and M r 24 500 membrane polypeptides, respectively. The M r 26 000 polypeptide was identified as the major subunits of the light‐harvesting chlorophyll a/b ‐protein (LHCP) complex and the M r 24 500 component seems to be functionally connected with this complex. From the results it is concluded that the chloroplast ATP synthetase consists of the subunit of the α, β, γ, δ, ϵ and III (proteolipid only and that proteolytically altered LHCP polypeptides bind artifically to the protein complex during isolation.